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CHMP4C belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. Additionally we are shipping CHMP4C Proteins (5) and many more products for this protein.
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Data demonstrate the biological importance of the abscission checkpoint and suggest that dysregulation of abscission by CHMP4CT232 may synergize with oncogene-induced mitotic stress to promote genomic instability and tumorigenesis.
Results show that CHMP4C, under the regulation of the chromosomal passenger complex, binds to highly curved membranes and promotes the closure of membrane gaps. Two distinctly localized pools of phosphorylated CHMP4C exist during cytokinesisI but the phosphorylation is not required for its assembly into spiral filaments. Also, the centralspindlin complex associates preferentially with the with unphosphorylated form.
CHMP4C mediates radiation resistance in lung cancer cells.
The ESCRT-III subunit CHMP4B is a key effector in abscission, whereas its paralogue, CHMP4C, is a component in the abscission checkpoint that delays abscission until chromatin is cleared from the intercellular bridge.
AURKB phosphorylates CHMP4C at 3 serines its C-terminal tail.Phosphorylation at these sites appears essential for CHMP4C function because their mutation leads to cytokinesis defects.
Single nucleotide polymorphisms in CHMP4C gene is associated with ovarian cancer.
findings show CHMP4C is involved in abscission timing; this function correlated with its differential spatiotemporal distribution during late stages of cytokinesis; CHMP4C functioned in the Aurora B-dependent abscission checkpoint
The Bro1 domain of ALIX binds specifically to C-terminal residues of the human CHMP4C.
CHMP4C belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (MIM 164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006
Snf7 homologue associated with Alix 3
, charged multivesicular body protein 4c
, chromatin modifying protein 4C
, chromatin-modifying protein 4c
, SNF7 homolog associated with Alix 3
, vacuolar protein sorting-associated protein 32-3
, charged multivesicular body protein 4C
, Chromatin-modifying protein 4c